Abstract
Salmonella is a well-known food-borne pathogen causing disease in humans and animals worldwide. Peptidyl-prolyl isomerases (PPIases) catalyse the cis–trans isomerisation of prolyl bound, which is a slow and rate-limiting step of protein folding. Here, we present the biochemical and molecular characterisation of a novel multi-domain parvulin-type, PPIases-C from the pathogenic bacteria Salmonella Typhimurium, annotated as rPpiC. The recombinant plasmid PpiC_pET28c was used for protein induction using 1.5 mM concentration of isopropyl-β-D-thiogalactopyranoside at 30 °C. Subsequently, the protein was identified by using the LC–MS technique showing high match score and sequence coverage with available PPIases-C proteins database. Using the succinyl-ala-phe-pro-phe-p nitroanilide as a substrate, Vmax of the enzyme was found to be 0.8187 ± 0.1352 µmoles/min and Km = 1.6014 ± 0.8449 µM, respectively. With this, we conclude that rPpiC protein is an active form of protein from Salmonella Typhimurium and plays an important role in protein folding.
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The authors are thankful to the SHUATS for providing the necessary funds and facilities for the current study.
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MK, IK and SA designed the experiments and carried out the experimental work. All authors were involved in scientific discussion and analysis of the data. All authors read and approved the final manuscript.
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Kumawat, M., Singh, R., Karuna, I. et al. Salmonella Typhimurium peptidyl-prolyl cis–trans isomerase C (PPIase C) plays a substantial role in protein folding to maintain the protein structure. World J Microbiol Biotechnol 36, 168 (2020). https://doi.org/10.1007/s11274-020-02943-x
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DOI: https://doi.org/10.1007/s11274-020-02943-x